Research

The research in my laboratory is focused on the molecular mechanisms of various histone modifications regulate the chromatin structure and in turn mediate different cellular processes.

Particular emphasis will be devoted to identify and characterize novel histone-modifying enzymes and regulatory proteins which mediate downstream effects and chromatin organization. The long term goal of this research is to understand the role of these epigenetic modifications in various diseases, particularly in human cancer. Using an activity-based biochemical approach, I have identified and characterized several histone-modifying enzymes including SET domain-containing histone H4K20 methyltransferase SET8 and Jmjc domain-containing histone H3K36 demethylase JHDM1. I also demonstrated that different polycomb group protein complexes PRC1 and PRC2, and their mediated histone H2A-K119 ubiquitination and histone H3-K27 methylation play important roles in X chromosome inactivation. The ongoing studies are to further dissect the molecular mechanism of histone H4-K20 methylation, demethylation and their potential roles in tumorigenesis. The lab is also interested in elucidating the role of histone modifications in various processes including transcriptional regulation,heterochromatin formation and X chromosome inactivation.